3EGG

Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1) and the PP1 binding and PDZ domains of Spinophilin

Summary for 3EGG

Entry DOI	10.2210/pdb3egg/pdb
Related	1FJM 1S70 2G5M 3E7A 3EGH 3HVQ
Descriptor	Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, Spinophilin, GLYCEROL, ... (6 entities in total)
Functional Keywords	pp1, spinophilin, serine/threonine phosphatase, post synaptic density, glutametergic receptors, carbohydrate metabolism, cell cycle, cell division, glycogen metabolism, hydrolase, iron, manganese, metal-binding, phosphoprotein, protein phosphatase, actin-binding, cell junction, cell projection, cytoskeleton, developmental protein, differentiation, neurogenesis, nucleus, synapse
Biological source	Homo sapiens (Human) More
Cellular location	Cytoplasm: P62136 Cytoplasm, cytoskeleton: O35274
Total number of polymer chains	4
Total formula weight	113395.08
Authors	Ragusa, M.J.,Page, R.,Peti, W. (deposition date: 2008-09-10, release date: 2010-03-23, Last modification date: 2023-08-30)
Primary citation	Ragusa, M.J.,Dancheck, B.,Critton, D.A.,Nairn, A.C.,Page, R.,Peti, W. Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nat.Struct.Mol.Biol., 17:459-464, 2010 Cited by PubMed: 20305656 DOI: 10.1038/nsmb.1786 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.85 Å)

Structure validation